2.7.7.2: FAD synthase
This is an abbreviated version!
For detailed information about FAD synthase, go to the full flat file.
Word Map on EC 2.7.7.2
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2.7.7.2
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desaturase
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polyunsaturated
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arachidonic
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docosahexaenoic
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linoleic
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eicosapentaenoic
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desaturation
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elongase
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elovl2
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omega-6
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delta-5
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lcpufas
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ammoniagenes
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srebf1
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gene-diet
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flavokinase
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synthesis
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nutrition
- 2.7.7.2
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desaturase
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polyunsaturated
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arachidonic
-
docosahexaenoic
-
linoleic
-
eicosapentaenoic
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desaturation
- elongase
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elovl2
-
omega-6
-
delta-5
-
lcpufas
- ammoniagenes
-
srebf1
-
gene-diet
- flavokinase
- synthesis
- nutrition
Reaction
Synonyms
adenosine triphosphate-riboflavin mononucleotide transadenylase, adenosine triphosphate-riboflavine mononucleotide transadenylase, ATP-FMN adenylyltransferase, ATP:FMN adenylyl transferase, ATP:FMN adenylyltransferase, AtRibF1, AtRibF2, FAD pyrophosphorylase, FAD synthase, FAD synthetase, FAD synthetase isoform 1, FAD synthetase isoform 2, Fad1, FADS, FADS-6, FADS1, FADS2, FLAD1, flavin adenine dinucleotide synthetase, FMN adenylyltransferase, FMN pyrophosphorylase, FMN:ATP adenylyltransferase, FMNAT, lysZ, MJ1179, More, ribF, RibL, riboflavin adenine dinucleotide pyrophosphorylase, riboflavin mononucleotide adenylyltransferase, riboflavine adenine dinucleotide adenylyltransferase, SPAP_1083
ECTree
2.7.7.2 FAD synthaseAdvanced search results
results (
results (KM Value
KM Value on EC 2.7.7.2 - FAD synthase
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KM VALUE [mM] 
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
0.48
CTP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.116
roseoflavin mononucleotide
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with 24 mM Na2S2O4, in 50 mM potassium phosphate (pH 7.5), at 37°C
0.025
ATP
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.03568
ATP
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wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0382
ATP
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mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0387
ATP
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mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0435
ATP
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FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.04537
ATP
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mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.04647
ATP
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mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.04704
ATP
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mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.07667
ATP
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mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.079
ATP
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FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.121
ATP
pH not specified in the publication, temperature not specified in the publication
0.0005
FMN
pH and temperature not specified in the publication, mutant N62A
0.00088
FMN
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mutant enzyme E268A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00088
FMN
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mutant enzyme T208D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00095
FMN
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mutant enzyme T208A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.001
FMN
pH and temperature not specified in the publication, wild-type enzyme
0.0011
FMN
pH and temperature not specified in the publication, mutant N62S
0.00117
FMN
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mutant enzyme E268D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.00119
FMN
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wild type enzyme, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0015
FMN
pH and temperature not specified in the publication, mutant D181A
0.0023
FMN
pH and temperature not specified in the publication, mutant R300A
0.003
FMN
pH and temperature not specified in the publication, mutant R297A
0.0054
FMN
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FADS monomer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.0071
FMN
pH and temperature not specified in the publication, mutant D168A
0.00823
FMN
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mutant enzyme N210A, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0093
FMN
pH and temperature not specified in the publication, mutant R297A/R300A
0.01501
FMN
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mutant enzyme N210D, at 37°C in 20 mM PIPES pH 7.0, 10 mM MgCl2
0.0311
FMN
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FADS trimer, 10 mM MgCl2 in 50 mM TrisHCl (pH 8.0), at 37°C
0.047
FMN
pH not specified in the publication, temperature not specified in the publication
0.063
FMN
apparent value, in 35 mM TES (K+) buffer (pH 7.2) containing 14 mM dithiothreitol, 7 mM MgCl+, at 70°C
0.1994
FMN
pH and temperature not specified in the publication, mutant W184A
additional information
additional information
R297A mutant protein: increased apparent KM-values for ATP and FMN by about 5 and 3times, respectively, compared to the wild-type enzyme
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additional information
additional information
MichaelisMenten model
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additional information
additional information
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MichaelisMenten model
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additional information
additional information
steady-state kinetic analysis of wild-type and mutant enzymes. The enzyme from Candida glabrata apparently binds its substrates with high affinity, but the overall turnover rate is very slow due to product inhibition
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